A bacterial enzyme degrading the model lignin compound β-etherase is a member of the glutathione- S-transferase superfamily

• Published in: FEBS letters Vol. 323; no. 1; pp. 135 - 140
• Main Authors: Masai, Eiji, Katayama, Yoshihiro, Kubota, Sachiko, Kawai, Shinya, Yamasaki, Makari, Morohoshi, Noriyuki
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 24.05.1993; Elsevier
• Subjects: Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Arylglycerol-β-aryl ether linkage; Bacterial Proteins; Base Sequence; Biological and medical sciences; Cloning, Molecular; Deoxyribonucleases, Type II Site-Specific - metabolism; DNA, Bacterial; Enzymes and enzyme inhibitors; Escherichia coli; Fundamental and applied biological sciences. Psychology; Glutathione - metabolism; Glutathione Transferase - metabolism; Glutathione- S-transferase; IPTG, isopropyl-β-D-thiogalactopyranoside; Lignin - metabolism; Lignin degradation; Molecular Sequence Data; NADH, reduced nicotinamide adenine dinucleotide; NADPH, reduced nicotinamide adenine dinucleotide phosphate; Oxidoreductases - genetics; Oxidoreductases - metabolism; Pseudomonas - enzymology; Pseudomonas paucimobilis; Restriction Mapping; Sequence Homology, Amino Acid; Transferases; β-Etherase; NADPH, reduced nicotinamide adenine dinucleotide phosphate; β-Etherase; IPTG, isopropyl-β-D-thiogalactopyranoside; Lignin degradation; NADH, reduced nicotinamide adenine dinucleotide; Pseudomonas paucimobilis; Arylglycerol-β-aryl ether linkage; Glutathione- S-transferase; Pseudomonadales; Enzymatic activity; Nucleotide sequence; Enzyme; Glutathione transferase; Bacteria; Pseudomonadaceae; Pseudomonas; Ligninolytic enzyme
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(93)81465-C

Cleavage of β-aryl ether linkages is essential in lignin degradation. We identified another β-etherase gene ( ligF), which contains an open reading frame of 771 bp and lies between genes coding Cα-dehydrogenase ( ligD) and β-etherase ( ligE). The β-etherase activity of LigF expressed in Escherichia coli was more than 80 times as high as that of LigE. ligF and ligE are homologous to glutathione- S-transferase, and upon addition of glutathione a remarkable acceleration of β-etherase activity was found in E. coli carrying ligF. It is concluded that LigF plays a central role in β-aryl ether cleavage and that glutathione is the hydrogen donor in this reaction.